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Targeted regulation of hygroscopicity of soybean antioxidant pentapeptide powder by zinc ions binding to the moisture absorption sites

文献作者：Peiyu Xue, Na Sun, Yong Li, Sheng Cheng, Songyi Lin   《Food Chemistry》

ABSTRACTS
In the present study, a targeted regulation of hygroscopicity of soybean antioxidant pentapeptide (SAP) powder was explored by zinc ions binding to its moisture absorption sites. Scanning electron microscopy, X-ray diffraction analysis, Fourier transform infrared spectroscopy and an energy-dispersive X-ray spectroscope were used to confirm the formation of the SAP-zinc complex. The results showed that morphology of SAP-zinc complex belonged to crystalline nanoparticles. The moisture sorption/desorption kinetics of the SAP-zinc complex changed compared to that of the SAP. In particular, the moisture sorption capacity of the SAP decreased and the distribution of adsorbed water changed after zinc chelation. Based on the binding of zinc ions to the moisture absorption sites, the hygroscopicity of SAP powder could be target regulated. Thus, this study could provide a new method to regulate the hygroscopicity of peptide powder.
KEY WORDS
Soybean antioxidant pentapeptide (SAP); Zinc chelation; Hygroscopicity; Targeted regulation.
SCREENSHOT

RELATED PRODUCTS
The SAP, Ser-His-Cys-Met-Asn, derived from soybean protein was synthesized by China Peptides Co., Ltd. (Shanghai, China) by solid-phase peptide synthesis method with 98.85% purity
CHAINING
https://www.sciencedirect.com/science/article/pii/S0308814617314644
Number of Residues:5
1-Letter Code:SHCMN
3-Letter Code:Ser-His-Cys-Met-Asn

Molecular weight (Mr):590.68 g/mol
Isoelectric point:7.2
Net charge at pH 7.0:0.0
Average hydrophilicity:-0.4
Ratio of hydrophilic residues / total number of residues:40 %

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